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SUMMARY:SAXS study of Escherichia coli Dihydrolipoamide Dehydrogenase: str
 uctural characteristics and molecular docking
DTSTART;VALUE=DATE-TIME:20160705T090000Z
DTEND;VALUE=DATE-TIME:20160705T100000Z
DTSTAMP;VALUE=DATE-TIME:20260416T200830Z
UID:indico-contribution-1173@indico.inp.nsk.su
DESCRIPTION:Speakers: Eleonora Shtykova (1. Shubnikov Institute of Crystal
 lography of Federal Scientific Research Centre “Crystallography and Phot
 onics” of Russian Academy of Sciences\, Moscow\, 119333 Russia\; 2. Mosc
 ow State University\, Moscow\, 119992 Russia)\nDihydrolipoamide dehydrogen
 ase from Escherichia coli (LpD) is a bacterial enzyme that is involved in 
 three different multi-enzyme complexes that catalyze similar decarboxylati
 on reactions of 2-oxoacids. All of these complexes comprise three enzymes 
 known as Е1\, Е2\, and Е3\, where LpD is the Е3 component and the E2 s
 ubunit is used by LpD as the lipoamide-containing protein substrate. The 
 Е1 and Е2 subunits have different structures in different complexes\, wh
 ereas the Е3 protein is essentially the same in all of the complexes [1
 –4]. The pyruvate dehydrogenase complex from Gram-negative bacteria (for
  example\, from E. coli) is composed of 24 E1 subunits and 24 E2 subunits\
 , whereas the multiplicity of E3 remains unknown. According to different e
 stimates\, there are 12 or 24 E3 subunits\; i.e.\, E3 may consist of six d
 imers or six tetramers.  It was shown that E. coli LpD exists as a dimer i
 n the crystalline state [5]. However\, the solution structure of this prot
 ein was unknown. The aim of the present study is to investigate the behavi
 or of LpD in solution\, i.e.\, under near-physiological conditions\, by sm
 all-angle X-ray scattering (SAXS) and complementary methods. Using modern 
 techniques for the interpretation of SAXS data and analytical ultracentrif
 ugation we determined that in solution LpD exists as an equilibrium mixtur
 e of a dimer and a tetramer.  The tetramer structure was determined by mod
 eling SAXS data and molecular docking. The results obtained by these two m
 ethods correlate well with each other. It was shown that there is the rela
 tionship between the oligomerization of the protein in solution and its fu
 nctional properties. In particular\, the possible flexibility of the tetra
 mer follows from the stoichiometric and functional demands of the multienz
 yme complexes containing LpD as a component.\n\nThis work was supported in
  part by Russian Foundation for Basic Researches (projects 15-54-74002 EMB
 L_а \, 15-04-01406\, 15-04-00563).\n\nReferences\n[1] R. H. Behall\, M. S
 . De Buysere\, B. Demeler\, et al.\, J.Biol. Chem. 269\, 31372 (1994).\n[2
 ] H. Lindsay\, E. Beaumont\, S. D. Richards\, et al.\, J. Biol. Chem. 275\
 , 36665 (2000).\n[3] W. Wei\, H. Li\, N. Nemeria\, and F. Jordan\, Protein
  Expr. Purif. 28\, 140 (2003).\n[4] M. A. Moxley\, D. A. Beard\, and J. N.
  Bazil\, Biophys. J. 107\, 2993 (2014).\n[5] K. Chandrasekhar\, J. Wang\, 
 P. Arjunan\, et al.\, J. Biolog. Chem. 288\, 15402 (2013).\n\nhttps://indi
 co.inp.nsk.su/event/3/contributions/1173/
LOCATION:Budker INP 2nd and 3rd floors
URL:https://indico.inp.nsk.su/event/3/contributions/1173/
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